View source for 9v6a


==X-ray crystal structure of the T66V mutant b5R co-crystallized with NADH==
<StructureSection load='9v6a' size='340' side='right'caption='[[9v6a]], [[Resolution|resolution]] 0.94&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9v6a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9V6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9V6A FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.94&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9v6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9v6a OCA], [https://pdbe.org/9v6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9v6a RCSB], [https://www.ebi.ac.uk/pdbsum/9v6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9v6a ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NB5R3_PIG NB5R3_PIG] Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.[:]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many structural studies have been reported for ferredoxin:NADP(+) reductase family members, but an experimental validation of the catalytic hydride and proton transfer steps through a direct detection of the involved hydrogen atoms has not been achieved so far. Here, we determined high-resolution X-ray and neutron crystal structures of NADH-cytochrome b(5) reductase, which acts as an electron supplier for various metabolic processes and mediates hydride and proton transfer reactions via its FAD and NADH cofactors. The X-ray structures identify the FADH(-)-NAD(+) and FAD-NADH complexes based on the electron densities of the hydrogen atoms bound to the cofactors. The neutron structures determined at different pD-values show a difference in the protonation state of the histidine residue in the hydrogen-bond network from FAD to the protein surface. The observation of the hydrogen atoms reveals the structural basis for the hydride and proton transfer reactions catalyzed by NADH-cytochrome b(5) reductase.

Structural basis of hydride and proton transfer reactions revealed by the detection of hydrogen atoms in mammalian NADH-cytochrome b(5) reductase.,Hirano Y, Kurihara K, Kusaka K, Ostermann A, Hikita M, Kimura S, Miki K, Tamada T Structure. 2025 Oct 30:S0969-2126(25)00393-4. doi: 10.1016/j.str.2025.10.006. PMID:41172987<ref>PMID:41172987</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9v6a" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Hikita M]]
[[Category: Hirano Y]]
[[Category: Kimura S]]
[[Category: Kurihara K]]
[[Category: Kusaka K]]
[[Category: Miki K]]
[[Category: Ostermann A]]
[[Category: Tamada T]]